Difference between revisions of "LmrB"

From SubtiWiki
Jump to: navigation, search
Line 140: Line 140:
<big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J''  </big>
<pubmed>15317768,17483215,12499232, 21815947 </pubmed>
<big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big>
<big>Mol Microbiol. 2011 81(6): 1459-1473. </big>
[http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947]
<pubmed>15317768,17483215,12499232, </pubmed>
[[Category:Protein-coding genes]]
[[Category:Protein-coding genes]]

Revision as of 16:07, 13 July 2013

  • Description: lincomycin-resistance protein (multidrug resistance pump)

Gene name lmrB
Synonyms yccA
Essential no
Product lincomycin-resistance protein
Function resistance to lincomycin
Gene expression levels in SubtiExpress: lmrB
MW, pI 51 kDa, 9.703
Gene length, protein length 1437 bp, 479 aa
Immediate neighbours ycbU, lmrA
Sequences Protein DNA DNA_with_flanks
Genetic context
LmrB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LmrB expression.png

Categories containing this gene/protein

transporters/ other, resistance against toxins/ antibiotics, membrane proteins

This gene is a member of the following regulons

LmrA regulon

The gene

Basic information

  • Locus tag: BSU02670

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: EmrB family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • induced by flavonoids such as quercetin (LmrA)PubMed
  • Regulatory mechanism:
  • Additional information:
    • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks


Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

Kazutake Hirooka, Satoshi Kunikane, Hiroshi Matsuoka, Ken-Ichi Yoshida, Kanako Kumamoto, Shigeo Tojo, Yasutaro Fujita
Dual regulation of the Bacillus subtilis regulon comprising the lmrAB and yxaGH operons and yxaF gene by two transcriptional repressors, LmrA and YxaF, in response to flavonoids.
J Bacteriol: 2007, 189(14);5170-82
[PubMed:17483215] [WorldCat.org] [DOI] (P p)

Ken-Ichi Yoshida, Yo-Hei Ohki, Makiko Murata, Masaki Kinehara, Hiroshi Matsuoka, Takenori Satomura, Reiko Ohki, Miyuki Kumano, Kunio Yamane, Yasutaro Fujita
Bacillus subtilis LmrA is a repressor of the lmrAB and yxaGH operons: identification of its binding site and functional analysis of lmrB and yxaGH.
J Bacteriol: 2004, 186(17);5640-8
[PubMed:15317768] [WorldCat.org] [DOI] (P p)

Miyuki Kumano, Masaya Fujita, Kouji Nakamura, Makiko Murata, Reiko Ohki, Kunio Yamane
Lincomycin resistance mutations in two regions immediately downstream of the -10 region of lmr promoter cause overexpression of a putative multidrug efflux pump in Bacillus subtilis mutants.
Antimicrob Agents Chemother: 2003, 47(1);432-5
[PubMed:12499232] [WorldCat.org] [DOI] (P p)